DSpace
 

DSpace at IIT Bombay >
IITB Publications >
Proceedings papers >

Please use this identifier to cite or link to this item: http://dspace.library.iitb.ac.in/jspui/handle/100/1275

Title: Thermal unfolding of hen egg-white lysozyme in the presence of 4-chlorobutan-1-ol
Authors: KISHORE, N
SABULAL, B
Keywords: differential scanning calorimetry
partially folded state
protein
trifluoroethanol
stability
models
Issue Date: 1998
Publisher: BLACKWELL SCIENCE LTD
Citation: PURE AND APPLIED CHEMISTRY,70(3)665-670
Abstract: High sensitivity differential scanning calorimetry transitions for the highly irreversible thermal denaturation of hen egg white lysozyme in the presence of low concentration (<250 mM) of 4-chlorobutan-1-ol are strongly scanning rate dependent, suggesting that the denaturation is at least in part, under kinetic control The scan rate dependence can be examined by assuming that the thermal denaturation takes place to the kinetic scheme [GRAPHICS] where k(3) >> k(2), thus the data fitting to the extreme case of this model ie. N --> F where N is the native state, D is the unfolded one and F is the final irreversibly arrived state. However, the thermal denaturation in the presence of 3-chloro-propan- 1-ol, 3-chloropropan-1,2-diol and their corresponding normal alcohols was earlier(ref 1) observed to be reversible two-state.
URI: http://dx.doi.org/10.1351/pac199870030665
http://dspace.library.iitb.ac.in/xmlui/handle/10054/14463
http://hdl.handle.net/100/1275
ISSN: 0033-4545
Appears in Collections:Proceedings papers

Files in This Item:

There are no files associated with this item.

View Statistics

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.

 

Valid XHTML 1.0! DSpace Software Copyright © 2002-2010  Duraspace - Feedback